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Related Experiment Videos

Evidence for multiple differing cation binding sites on hemoglobin A and S.

G Amiconi, L Civalleri, S G Condò

    Hemoglobin
    |January 1, 1981
    PubMed
    Summary

    Divalent cations like calcium and zinc bind to hemoglobin, influencing its oxygen affinity. Hemoglobin S has a unique cation binding site due to structural changes.

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    Area of Science:

    • Biochemistry
    • Protein Chemistry
    • Molecular Biology

    Background:

    • Divalent cations can interact with proteins, potentially modulating their function.
    • Hemoglobin structure and function are sensitive to environmental factors and mutations.

    Purpose of the Study:

    • To investigate the interaction of divalent cations with normal and sickle cell hemoglobin.
    • To understand how cation binding affects hemoglobin's oxygen affinity and conformation.

    Main Methods:

    • Studying the effect of calcium (Ca++), zinc (Zn++), and nickel (Ni++) on hemoglobin oxygen affinity.
    • Analyzing cation binding preferences for different hemoglobin conformations (oxy- vs. deoxy-).

    Main Results:

    • Ca++ and Zn++ preferentially bind to the oxy-conformation of hemoglobin S and normal hemoglobin, respectively.

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  • Ni++ binding reduces oxygen affinity in both normal and sickle cell hemoglobin.
  • Evidence suggests at least two distinct cation binding sites on hemoglobin.
  • The glutamic acid to valine substitution in hemoglobin S creates a novel cation binding site.

    • Conclusions:

    • Divalent cations act as oxygen-linked ligands for hemoglobin.
    • Structural alterations in hemoglobin S create unique cation binding properties.
    • Cation binding can allosterically modulate hemoglobin's oxygen transport function.